Issue 1, 2009
From the journal:

Physical Chemistry Chemical Physics

Collapse transition in proteins

Guy Ziv,a   D. Thirumalaib  and  Gilad Haran*a  

* Corresponding authors

a Chemical Physics Department, Weizmann Institute of Science, Rehovot, Israel
E-mail: gilad.haran@weizmann.ac.il

b Biophysics Program, Institute for Physical Science and Technology and Department of Chemistry and Biochemistry, University of Maryland, College Park, USA

Abstract

The coil–globule transition, a tenet of the physics of polymers, has been identified in recent years as an important unresolved aspect of the initial stages of the folding of proteins. We describe the basics of the collapse transition, starting with homopolymers and continuing with proteins. Studies of denatured-state collapse under equilibrium are then presented. An emphasis is placed on single-molecule fluorescence experiments, which are particularly useful for measuring properties of the denatured state even under conditions of coexistence with the folded state. Attempts to understand the dynamics of collapse, both theoretically and experimentally, are then described. Only an upper limit for the rate of collapse has been obtained so far. Improvements in experimental and theoretical methodology are likely to continue to push our understanding of the importance of the denatured-state thermodynamics and dynamics for protein folding in the coming years.

Graphical abstract: Collapse transition in proteins

About
Cited by
Related
Download options Please wait...

Article information

DOI
https://doi.org/10.1039/B813961J
Article type
Perspective
Submitted
12 Aug 2008
Accepted
13 Oct 2008
First published
14 Nov 2008

Phys. Chem. Chem. Phys., 2009,11, 83-93

Permissions

Request permissions

Collapse transition in proteins

G. Ziv, D. Thirumalai and G. Haran, Phys. Chem. Chem. Phys., 2009, 11, 83 DOI: 10.1039/B813961J

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements